ID A0A1G5UQ00_9SPHN Unreviewed; 1104 AA.
AC A0A1G5UQ00;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273, ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=SAMN03159340_03341 {ECO:0000313|EMBL:SDA35723.1};
OS Sphingomonas sp. NFR15.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1566282 {ECO:0000313|EMBL:SDA35723.1, ECO:0000313|Proteomes:UP000199327};
RN [1] {ECO:0000313|Proteomes:UP000199327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR15 {ECO:0000313|Proteomes:UP000199327};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC translesion synthesis (TLS). It is not the major replicative DNA
CC polymerase. {ECO:0000256|HAMAP-Rule:MF_01902}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_01902};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391, ECO:0000256|HAMAP-
CC Rule:MF_01902}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMWX01000008; SDA35723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5UQ00; -.
DR STRING; 1566282.SAMN03159340_03341; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199327; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07434; PHP_PolIIIA_DnaE2; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01902; DNApol_error_prone; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR023073; DnaE2.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01902};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_01902};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01902}; Reference proteome {ECO:0000313|Proteomes:UP000199327};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1104 AA; 123588 MW; BCA7EEBC1572BF6A CRC64;
MTSDARYVEL QVTTHFSFLR GASSPEELFA AAVLLRLPAL GIVDRSSVAG IVRAWDAEKT
TGVRSIIGSR IDLVDGTALL LYPTDRAAYG RMCRLLSVGK ERAGKGACHL DWPDVEQWHE
GLIAILAPDR ADTVAEGALA RAKRIFQDRL YLALSIRRRP KDAIRLRDLA NIAAAARVPT
VATNDVLYHS PDRRMLQDVV TCVRERCTID ELGDRRERFA DRYLKAGEEM ERLFRRYLKD
ATPVFRTLEV AKRCTFSLEE LRYQYPDEIS VPGRTPQEEL ERLTWAKAPE RYPEGIEGKV
HTQLEHELKL IADLEYAPYF LTVHSIVAEA RRREIICQGR GSAANSAVCY VLGITSIDPV
RSELLFERFV SAERREPPDI DVDFEHERRE EVIQWIYETY GRTRSALTAV VTRYRARGAV
RDVGKALGLS EDMTAGLSSA VWSWSREGVE EKHAEELNMD LSDRRLALTL ELARQLINTP
RHLSQHPGGF VLTRDRLDEL VPIEPAAMED RQVIEWDKDD IDLLGFMKVD VLALGMLSCM
RRAFEFLEND KGLKLDLATI PAEDPATYAM IRKADTLGVF QIESRAQMAS IPLMAPRTFY
DLVIQVAIVR PGPIQGDMVH PYRRRRNGEE EVTYPTEELR RVLEKTLGVP LFQEQAMRVA
IECAGFTASE ADLLRRAMAT FKLTGGVSHF RDKLIDGMVS RGYDQEFAER TFKQIEGFGS
YGFPESHAAS FALIAYASSW MKCHHPDVFC AALLNAQPMG FYAPAQIVRD ARQHGVEIRP
IDVNHSRWDC TLEPAGGRYL AVRLGLRMVR DLANGDAASI VTARANTPYE SIEEIQRRAG
VGRGALDRIG EADGFGSLGS NRREGLWSVK GLGNAALPLF AAADEREGKL RAEAIEPTVI
LAPMGEGAEV VEDYRASGLS LRAHPLAFLR DELRARKMIT CEELQTVRDG RWINLAGIVL
VRQKPGSAKG VMFITLEDET NVANLVVWTN VFEKHRRIVL GASMMGVRGQ VQREGNVIHV
IAQRLDDLSP SLATVGNRAD VADIYRTSRA DIVKSPVGPD PRDPARAPLG RQPRDIFIPD
LRLGSGIIPG QLTEGIKVKP RDFR
//
